| Year |
Citation |
Score |
| 2014 |
Erlendsson S, Rathje M, Heidarsson PO, Poulsen FM, Madsen KL, Teilum K, Gether U. Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligands. The Journal of Biological Chemistry. 289: 25327-40. PMID 25023278 DOI: 10.1074/Jbc.M114.548743 |
0.629 |
|
| 2014 |
Ozenne V, Noel JK, Heidarsson PO, Brander S, Poulsen FM, Jensen MR, Kragelund BB, Blackledge M, Danielsson J. Exploring the minimally frustrated energy landscape of unfolded ACBP. Journal of Molecular Biology. 426: 722-34. PMID 24211721 DOI: 10.1016/J.Jmb.2013.10.031 |
0.41 |
|
| 2013 |
Iešmantavi?ius V, Jensen MR, Ozenne V, Blackledge M, Poulsen FM, Kjaergaard M. Modulation of the intrinsic helix propensity of an intrinsically disordered protein reveals long-range helix-helix interactions. Journal of the American Chemical Society. 135: 10155-63. PMID 23758617 DOI: 10.1021/ja4045532 |
0.366 |
|
| 2013 |
Kenchappa CS, Heidarsson PO, Kragelund BB, Garrett RA, Poulsen FM. Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2. Nucleic Acids Research. 41: 3424-35. PMID 23325851 DOI: 10.1093/nar/gks1465 |
0.356 |
|
| 2012 |
Gjerstorff MF, Rösner HI, Pedersen CB, Greve KB, Schmidt S, Wilson KL, Mollenhauer J, Besir H, Poulsen FM, Møllegaard NE, Ditzel HJ. GAGE cancer-germline antigens are recruited to the nuclear envelope by germ cell-less (GCL). Plos One. 7: e45819. PMID 23029259 DOI: 10.1371/Journal.Pone.0045819 |
0.307 |
|
| 2012 |
Heidarsson PO, Valpapuram I, Camilloni C, Imparato A, Tiana G, Poulsen FM, Kragelund BB, Cecconi C. A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway. Journal of the American Chemical Society. 134: 17068-75. PMID 23004011 DOI: 10.1021/Ja305862M |
0.393 |
|
| 2012 |
Kjaergaard M, Poulsen FM, Kragelund BB. Temperature-induced transitions in disordered proteins probed by NMR spectroscopy. Methods in Molecular Biology (Clifton, N.J.). 896: 233-47. PMID 22821528 DOI: 10.1007/978-1-4614-3704-8_15 |
0.321 |
|
| 2012 |
Kjaergaard M, Poulsen FM, Teilum K. Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered. Biophysical Journal. 102: 1627-35. PMID 22500763 DOI: 10.1016/J.Bpj.2012.02.014 |
0.688 |
|
| 2012 |
Heidarsson PO, Bjerrum-Bohr IJ, Jensen GA, Pongs O, Finn BE, Poulsen FM, Kragelund BB. The C-terminal tail of human neuronal calcium sensor 1 regulates the conformational stability of the Ca²âºâ‚‹ activated state. Journal of Molecular Biology. 417: 51-64. PMID 22227393 DOI: 10.1016/J.Jmb.2011.12.049 |
0.309 |
|
| 2011 |
Kjaergaard M, Iešmantavi?ius V, Poulsen FM. The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts. Protein Science : a Publication of the Protein Society. 20: 2023-34. PMID 21898648 DOI: 10.1002/pro.726 |
0.335 |
|
| 2011 |
Kjaergaard M, Poulsen FM. Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution. Journal of Biomolecular Nmr. 50: 157-65. PMID 21604143 DOI: 10.1007/s10858-011-9508-2 |
0.304 |
|
| 2010 |
Bruun SW, Iesmantavicius V, Danielsson J, Poulsen FM. Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein. Proceedings of the National Academy of Sciences of the United States of America. 107: 13306-11. PMID 20624986 DOI: 10.1073/pnas.1003004107 |
0.402 |
|
| 2010 |
Kjaergaard M, Teilum K, Poulsen FM. Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. Proceedings of the National Academy of Sciences of the United States of America. 107: 12535-40. PMID 20616042 DOI: 10.1073/Pnas.1001693107 |
0.677 |
|
| 2010 |
Rösner HI, Poulsen FM. Residue-specific description of non-native transient structures in the ensemble of acid-denatured structures of the all-beta protein c-src SH3. Biochemistry. 49: 3246-53. PMID 20218679 DOI: 10.1021/bi902125j |
0.395 |
|
| 2010 |
Poulsen F, Roesner H. backbone chemical shifts assignments of acid-denatured c-src SH3 with increasing urea concentration Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16750 |
0.302 |
|
| 2009 |
Andersen KK, Oliveira CL, Larsen KL, Poulsen FM, Callisen TH, Westh P, Pedersen JS, Otzen D. The role of decorated SDS micelles in sub-CMC protein denaturation and association. Journal of Molecular Biology. 391: 207-26. PMID 19523473 DOI: 10.1016/J.Jmb.2009.06.019 |
0.477 |
|
| 2008 |
Danielsson J, Liljedahl L, Bárány-Wallje E, Sønderby P, Kristensen LH, Martinez-Yamout MA, Dyson HJ, Wright PE, Poulsen FM, Mäler L, Gräslund A, Kragelund BB. The intrinsically disordered RNR inhibitor Sml1 is a dynamic dimer. Biochemistry. 47: 13428-37. PMID 19086274 DOI: 10.1021/Bi801040B |
0.398 |
|
| 2008 |
Modig K, Poulsen FM. Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP. Journal of Biomolecular Nmr. 42: 163-77. PMID 18850278 DOI: 10.1007/s10858-008-9280-0 |
0.331 |
|
| 2008 |
Teilum K, Kragelund BB, Poulsen FM. Application of Hydrogen Exchange Kinetics to Studies of Protein Folding Protein Folding Handbook. 2: 634-672. DOI: 10.1002/9783527619498.ch18 |
0.612 |
|
| 2007 |
Modig K, Jürgensen VW, Lindorff-Larsen K, Fieber W, Bohr HG, Poulsen FM. Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis. Febs Letters. 581: 4965-71. PMID 17910956 DOI: 10.1016/j.febslet.2007.09.027 |
0.379 |
|
| 2007 |
Kjaergaard M, Gårdsvoll H, Hirschberg D, Nielbo S, Mayasundari A, Peterson CB, Jansson A, Jørgensen TJ, Poulsen FM, Ploug M. Solution structure of recombinant somatomedin B domain from vitronectin produced in Pichia pastoris. Protein Science : a Publication of the Protein Society. 16: 1934-45. PMID 17766387 DOI: 10.1110/ps.072949607 |
0.303 |
|
| 2006 |
Nygaard R, Nielbo S, Schwartz TW, Poulsen FM. The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR. Biochemistry. 45: 8350-7. PMID 16819834 DOI: 10.1021/bi060359l |
0.326 |
|
| 2006 |
Teilum K, Poulsen FM, Akke M. The inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding protein. Proceedings of the National Academy of Sciences of the United States of America. 103: 6877-82. PMID 16641108 DOI: 10.1073/Pnas.0509100103 |
0.625 |
|
| 2005 |
Kristjansdottir S, Lindorff-Larsen K, Fieber W, Dobson CM, Vendruscolo M, Poulsen FM. Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies. Journal of Molecular Biology. 347: 1053-62. PMID 15784263 DOI: 10.1016/J.Jmb.2005.01.009 |
0.392 |
|
| 2005 |
Teilum K, Thormann T, Caterer NR, Poulsen HI, Jensen PH, Knudsen J, Kragelund BB, Poulsen FM. Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins. 59: 80-90. PMID 15690348 DOI: 10.1002/Prot.20340 |
0.606 |
|
| 2005 |
Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, ... ... Poulsen FM, et al. Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Science : a Publication of the Protein Society. 14: 602-16. PMID 15689503 DOI: 10.1110/Ps.041205405 |
0.64 |
|
| 2005 |
Fieber W, Kragelund BB, Meldal M, Poulsen FM. Reversible dimerization of acid-denatured ACBP controlled by helix A4. Biochemistry. 44: 1375-84. PMID 15683223 DOI: 10.1021/Bi0481949 |
0.383 |
|
| 2004 |
Nielbo S, Thomsen JK, Graversen JH, Jensen PH, Etzerodt M, Poulsen FM, Thøgersen HC. Structure of the plasminogen kringle 4 binding calcium-free form of the C-type lectin-like domain of tetranectin. Biochemistry. 43: 8636-43. PMID 15236571 DOI: 10.1021/bi049570s |
0.313 |
|
| 2004 |
Andersen P, Kragelund BB, Olsen AN, Larsen FH, Chua NH, Poulsen FM, Skriver K. Structure and biochemical function of a prototypical Arabidopsis U-box domain. The Journal of Biological Chemistry. 279: 40053-61. PMID 15231834 DOI: 10.1074/jbc.M405057200 |
0.367 |
|
| 2004 |
Fieber W, Kristjansdottir S, Poulsen FM. Short-range, long-range and transition state interactions in the denatured state of ACBP from residual dipolar couplings. Journal of Molecular Biology. 339: 1191-9. PMID 15178258 DOI: 10.1016/j.jmb.2004.04.037 |
0.392 |
|
| 2004 |
Lindorff-Larsen K, Kristjansdottir S, Teilum K, Fieber W, Dobson CM, Poulsen FM, Vendruscolo M. Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein. Journal of the American Chemical Society. 126: 3291-9. PMID 15012160 DOI: 10.1021/Ja039250G |
0.677 |
|
| 2004 |
Jensen PR, Axelsen JB, Lerche MH, Poulsen FM. Improvement of hydrogen bond geometry in protein NMR structures by residual dipolar couplings--an assessment of the interrelation of NMR restraints. Journal of Biomolecular Nmr. 28: 31-41. PMID 14739637 DOI: 10.1023/B:JNMR.0000012865.35872.cc |
0.304 |
|
| 2004 |
Nielbo S, Thomsen J, Jensen P, Graversen J, Etzerodt M, Poulsen F, Thogersen H. 1H, 13C and 15N resonance assignment of the Plasminogen Kringle 4 Binding Calcium Free Form of the C-type Lectin-like Domain of Tetranectin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr6007 |
0.31 |
|
| 2002 |
Groes M, Teilum K, Olesen K, Poulsen FM, Henriksen A. Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding domain of flocculin, a cell-adhesion molecule from Saccharomyces carlsbergensis. Acta Crystallographica. Section D, Biological Crystallography. 58: 2135-7. PMID 12454478 DOI: 10.1107/S0907444902015494 |
0.586 |
|
| 2002 |
Teilum K, Kragelund BB, Poulsen FM. Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling. Journal of Molecular Biology. 324: 349-57. PMID 12441112 DOI: 10.1016/S0022-2836(02)01039-2 |
0.67 |
|
| 2002 |
Teilum K, Maki K, Kragelund BB, Poulsen FM, Roder H. Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proceedings of the National Academy of Sciences of the United States of America. 99: 9807-12. PMID 12096190 DOI: 10.1073/Pnas.152321499 |
0.642 |
|
| 2002 |
Thomsen JK, Kragelund BB, Teilum K, Knudsen J, Poulsen FM. Transient intermediary states with high and low folding probabilities in the apparent two-state folding equilibrium of ACBP at low pH. Journal of Molecular Biology. 318: 805-14. PMID 12054824 DOI: 10.1016/S0022-2836(02)00159-6 |
0.657 |
|
| 2000 |
Teilum K, Kragelund BB, Knudsen J, Poulsen FM. Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP. Journal of Molecular Biology. 301: 1307-14. PMID 10966822 DOI: 10.1006/Jmbi.2000.4003 |
0.66 |
|
| 1999 |
Kragelund BB, Knudsen J, Poulsen FM. Acyl-coenzyme A binding protein (ACBP). Biochimica Et Biophysica Acta. 1441: 150-61. PMID 10570243 DOI: 10.1016/S1388-1981(99)00151-1 |
0.439 |
|
| 1999 |
Kragelund BB, Osmark P, Neergaard TB, Schiødt J, Kristiansen K, Knudsen J, Poulsen FM. The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP Nature Structural Biology. 6: 594-601. PMID 10360367 DOI: 10.1038/9384 |
0.444 |
|
| 1999 |
Kragelund BB, Poulsen K, Andersen KV, Baldursson T, Krøll JB, Neergård TB, Jepsen J, Roepstorff P, Kristiansen K, Poulsen FM, Knudsen J. Conserved residues and their role in the structure, function, and stability of acyl-coenzyme A binding protein Biochemistry. 38: 2386-2394. PMID 10029532 DOI: 10.1021/bi982427c |
0.394 |
|
| 1998 |
Lerche MH, Poulsen FM. Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins Protein Science. 7: 2490-2498. PMID 9865943 |
0.395 |
|
| 1998 |
Kragelund BB, Heinemann B, Knudsen J, Poulsen FM. Mapping the lifetimes of local opening events in a native state protein Protein Science. 7: 2237-2248. PMID 9827990 |
0.336 |
|
| 1997 |
Nielsen PR, Ellgaard L, Etzerodt M, Thøgersen HC, Poulsen FM. The solution structure of the N-terminal domain of α2-macroglobulin receptor-associated protein Proceedings of the National Academy of Sciences of the United States of America. 94: 7521-7525. PMID 9207124 DOI: 10.1073/pnas.94.14.7521 |
0.36 |
|
| 1997 |
Lerche MH, Kragelund BB, Bech LM, Poulsen FM. Barley lipid-transfer protein complexed with palmitoyl CoA: The structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands Structure. 5: 291-306. PMID 9032083 |
0.354 |
|
| 1996 |
Heinemann B, Andersen KV, Nielsen PR, Bech LM, Poulsen FM. Structure in solution of a four-helix lipid binding protein Protein Science. 5: 13-23. PMID 8771192 |
0.37 |
|
| 1996 |
Rischel C, Thyberg P, Rigler R, Poulsen FM. Time-resolved fluorescence studies of the molten globule state of apomyoglobin Journal of Molecular Biology. 257: 877-885. PMID 8636988 DOI: 10.1006/Jmbi.1996.0208 |
0.318 |
|
| 1996 |
Kragelund BB, Højrup P, Jensen MS, Schjerling CK, Juul E, Knudsen J, Poulsen FM. Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family Journal of Molecular Biology. 256: 187-200. PMID 8609609 DOI: 10.1006/jmbi.1996.0076 |
0.433 |
|
| 1995 |
Kragelund BB, Robinson CV, Knudsen J, Dobson CM, Poulsen FM. Folding of a four-helix bundle: Studies of acyl-coenzyme A binding protein Biochemistry. 34: 7217-7224. PMID 7766632 DOI: 10.1021/Bi00021A037 |
0.477 |
|
| 1995 |
Kragelund BB, Knudsen J, Poulsen FM. Local perturbations by ligand binding of hydrogen deuterium exchange kinetics in a four-helix bundle protein, acyl coenzyme A binding protein (ACBP) Journal of Molecular Biology. 250: 695-706. PMID 7623386 DOI: 10.1006/jmbi.1995.0409 |
0.408 |
|
| 1995 |
Rischel C, Poulsen FM. Modification of a specific tyrosine enables tracing of the end-to-end distance during apomyoglobin folding Febs Letters. 374: 105-109. PMID 7589493 DOI: 10.1016/0014-5793(95)01087-U |
0.304 |
|
| 1994 |
Nielsen PR, Einer-Jensen K, Holtet TL, Andersen BD, Poulsen FM, Thøgersen HC. Protein-ligand interactions in the lysine-binding site of plasminogen kringle 4 are different in crystal and solution. Electrostatic interactions studied by site-directed mutagenesis exclude Lys35 as an important acceptor in solution. Biochemistry. 32: 13019-25. PMID 8241155 DOI: 10.1021/bi00211a010 |
0.326 |
|
| 1994 |
Rischel C, Madsen JC, Andersen KV, Poulsen FM. Comparison of backbone dynamics of apo- and holo-acyl-coenzyme A binding protein using 15N relaxation measurements Biochemistry. 33: 13997-14002. PMID 7947808 |
0.335 |
|
| 1993 |
Kragelund BB, Andersen KV, Madsen JC, Knudsen J, Poulsen FM. Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A Journal of Molecular Biology. 230: 1260-1277. PMID 8503960 |
0.385 |
|
| 1993 |
Andersen KV, Poulsen FM. The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: Structural refinement using heteronuclear multidimensional NMR spectroscopy Journal of Biomolecular Nmr. 3: 271-284. PMID 8358232 DOI: 10.1007/BF00212514 |
0.352 |
|
| 1993 |
Knudsen J, Mandrup S, Rasmussen JT, Andreasen PH, Poulsen F, Kristiansen K. The function of acyl-CoA-binding protein (ACBP)/Diazepam binding inhibitor (DBI) Molecular and Cellular Biochemistry. 123: 129-138. PMID 8232254 DOI: 10.1007/978-1-4615-3096-1_17 |
0.345 |
|
| 1992 |
Ludvigsen S, Poulsen FM. Three-dimensional structure in solution of barwin, a protein from barley seed. Biochemistry. 31: 8783-9. PMID 1390665 DOI: 10.1021/bi00152a014 |
0.328 |
|
| 1992 |
Ludvigsen S, Poulsen FM. Secondary structure in solution of barwin from barley seed using 1H nuclear magnetic resonance spectroscopy. Biochemistry. 31: 8771-82. PMID 1390664 DOI: 10.1021/bi00152a013 |
0.353 |
|
| 1991 |
Andersen KV, Ludvigsen S, Mandrup S, Knudsen J, Poulsen FM. The secondary structure in solution of acyl-coenzyme A binding protein from bovine liver using 1H nuclear magnetic resonance spectroscopy. Biochemistry. 30: 10654-63. PMID 1931985 DOI: 10.1021/bi00108a008 |
0.375 |
|
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